N-acetyl-gamma-glutamyl-phosphate reductase (P11446)

Identification
Name:N-acetyl-gamma-glutamyl-phosphate reductase
Synonyms:
  • AGPR
  • N-acetyl-glutamate semialdehyde dehydrogenase
  • NAGSA dehydrogenase
Gene Name:argC
Enzyme Class:
Biological Properties
General Function:Involved in N-acetyl-gamma-glutamyl-phosphate reductase activity
Specific Function:N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = N-acetyl-5-glutamyl phosphate + NADPH
Cellular Location:Cytoplasm (Probable)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0N-Acetyl-L-glutamate 5-semialdehyde + 1.0NADP + 1.0Phosphate ↔ 1.0N-Acetyl-L-glutamyl 5-phosphate + 1.0Hydrogen ion + 1.0NADPH
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0NADPH+1.0Thumb+1.0Thumb → 1.0N-acetyl-L-glutamate+1.0Thumb+1.0Thumb
1.0N-Acetyl-L-glutamyl 5-phosphate + 1.0NADPH + 1.0Hydrogen ion + 1.0NADPH → 1.0N-acetyl-L-glutamate + 1.0Phosphate + 1.0NADP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0N-Acetyl-L-glutamate 5-semialdehyde + 1.0NADP + 1.0Phosphate ↔ 1.0N-Acetyl-L-glutamyl 5-phosphate + 1.0Hydrogen ion + 1.0NADPH
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0N-Acetyl-L-glutamate 5-semialdehyde + 1.0NADP + 1.0Inorganic phosphate → 1.0N-Acetyl-L-glutamyl 5-phosphate + 1.0NADPH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB06488N-Acetyl-L-glutamate 5-semialdehydeMetaboCard
ECMDB06456N-Acetyl-L-glutamyl 5-phosphateMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB01429PhosphateMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
binding
catalytic activity
N-acetyl-gamma-glutamyl-phosphate reductase activity
NAD or NADH binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on the aldehyde or oxo group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
protein binding
protein dimerization activity
Process
arginine biosynthetic process
arginine metabolic process
cellular amino acid and derivative metabolic process
cellular amino acid biosynthetic process
cellular amino acid metabolic process
cellular metabolic process
glutamine family amino acid metabolic process
metabolic process
Gene Properties
Blattner:b3958
Gene OrientationClockwise
Centisome Percentage:89.51
Left Sequence End4153024
Right Sequence End4154028
Gene Sequence:
>1005 bp
GTGAAACTGGATGAAATCGCTCGGCTGGCGGGAGTGTCGCGGACCACTGCAAGCTATGTT
ATTAACGGCAAAGCGAAGCAATACCGTGTGAGCGACAAAACCGTTGAAAAAGTCATGGCT
GTGGTGCGTGAGCACAATTACCACCCGAACGCCGTGGCAGCTGGGCTTCGTGCTGGACGC
ACACGTTCTATTGGTCTTGTGATCCCCGATCTGGAGAACACCAGCTATACCCGCATCGCT
AACTATCTTGAACGCCAGGCGCGGCAACGGGGTTATCAACTGCTGATTGCCTGCTCAGAA
GATCAGCCAGACAACGAAATGCGGTGCATTGAGCACCTTTTACAGCGTCAGGTTGATGCC
ATTATTGTTTCGACGTCGTTGCCTCCTGAGCATCCTTTTTATCAACGCTGGGCTAACGAC
CCGTTCCCGATTGTCGCGCTGGACCGCGCCCTCGATCGTGAACACTTCACCAGCGTGGTT
GGTGCCGATCAGGATGATGCCGAAATGCTGGCGGAAGAGTTACGTAAGTTTCCCGCCGAG
ACGGTGCTTTATCTTGGTGCGCTACCGGAGCTTTCTGTCAGCTTCCTGCGTGAACAAGGT
TTCCGTACTGCCTGGAAAGATGATCCGCGCGAAGTGCATTTCCTGTATGCCAACAGCTAT
GAGCGGGAGGCGGCTGCCCAGTTATTCGAAAAATGGCTGGAAACGCATCCGATGCCGCAG
GCGCTGTTCACAACGTCGTTTGCGTTGTTGCAAGGAGTGATGGATGTCACGCTGCGTCGC
GACGGCAAACTGCCTTCTGACCTGGCAATTGCCACCTTTGGCGATAACGAACTGCTCGAC
TTCTTACAGTGTCCGGTGCTGGCAGTGGCTCAACGTCACCGCGATGTCGCAGAGCGTGTG
CTGGAGATTGTCCTGGCAAGCCTGGACGAACCGCGTAAGCCAAAACCTGGTTTAACGCGC
ATTAAACGTAATCTCTATCGCCGCGGCGTGCTCAGCCGTAGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:334
Protein Molecular Weight:35952
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>N-acetyl-gamma-glutamyl-phosphate reductase
MLNTLIVGASGYAGAELVTYVNRHPHMNITALTVSAQSNDAGKLISDLHPQLKGIVDLPL
QPMSDISEFSPGVDVVFLATAHEVSHDLAPQFLEAGCVVFDLSGAFRVNDATFYEKYYGF
THQYPELLEQAAYGLAEWCGNKLKEANLIAVPGCYPTAAQLALKPLIDADLLDLNQWPVI
NATSGVSGAGRKAAISNSFCEVSLQPYGVFTHRHQPEIATHLGADVIFTPHLGNFPRGIL
ETITCRLKSGVTQAQVAQVLQQAYAHKPLVRLYDKGVPALKNVVGLPFCDIGFAVQGEHL
IIVATEDNLLKGAAAQAVQCANIRFGYAETQSLI
References
External Links:
ResourceLink
Uniprot ID:P11446
Uniprot Name:ARGC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321961
Ecogene ID:EG10065
Ecocyc:EG10065
ColiBase:b3958
Kegg Gene:b3958
EchoBASE ID:EB0063
CCDB:ARGC_ECOLI
BacMap:16131796
General Reference:
  • Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 21:5408-5417. Pubmed: 8265357
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Meinnel, T., Schmitt, E., Mechulam, Y., Blanquet, S. (1992). "Structural and biochemical characterization of the Escherichia coli argE gene product." J Bacteriol 174:2323-2331. Pubmed: 1551850
  • Parsot, C., Boyen, A., Cohen, G. N., Glansdorff, N. (1988). "Nucleotide sequence of Escherichia coli argB and argC genes: comparison of N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde dehydrogenase with homologous and analogous enzymes." Gene 68:275-283. Pubmed: 2851495
  • Piette, J., Cunin, R., Boyen, A., Charlier, D., Crabeel, M., Van Vliet, F., Glansdorff, N., Squires, C., Squires, C. L. (1982). "The regulatory region of the divergent argECBH operon in Escherichia coli K-12." Nucleic Acids Res 10:8031-8048. Pubmed: 6761650